Anti-Yellow Fever virus NS3 protein antibody [GT344] - BSA and Azide free

Target data

Capsid protein C. Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions.. Capsid protein C. Inhibits RNA silencing by interfering with host Dicer.. Peptide pr. Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.. Protein prM. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion loop. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.. Small envelope protein M. May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.. Envelope protein E. Type II fusion protein that binds to host cell surface receptor and mediates fusion between viral and cellular membranes (By similarity). The envelope protein E shifts from dimeric state to trimeric state to perform fusion with the host membrane (By similarity). The fusion loops of the three subunits come together to form a membrane-insertable tip containing aromatic residues (By similarity). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers of precursor prM and envelope protein E (By similarity). Envelope protein exposes a positively-charged pr-binding pocket at the E dimer interface, inducing (prM/E)2 dimer formation to generate smooth particles in the Golgi (By similarity). The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (By similarity). prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (By similarity). Pr is shed from the particle upon subsequent secretion into the extracellular environment, leaving an activated particle, prone to mediate acidic pH-triggered membrane fusion upon entry into a target cell (By similarity).. Non-structural protein 1. Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations : the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).. Non-structural protein 2A. Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.. Serine protease subunit NS2B. Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).. Serine protease NS3. Displays three enzymatic activities : serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm : C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (PubMed : 18199634).. Non-structural protein 4A. Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.. Peptide 2k. Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.. Non-structural protein 4B. Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (PubMed : 15956546).. RNA-directed RNA polymerase/Methyltransferase NS5. Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed : 19850911). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed : 19850911). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed : 25211074). IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition (PubMed : 25211074).

Alternative Names

Genome polyprotein